Measurement of the synthesis rates of collagens and total protein in rabbit muscle.
1. Collagen- and total-protein-synthesis rates were determined in rabbit muscle by continuous infusion of radioactive proline. 2. The precursor pool of free proline used for collagen synthesis was defined by measuring the specific radioactivity of hydroxy-proline in isolated type I procollagen. The specific radioactivities of type I procollagen were about 40% of those for free proline in the homogenate. 3. The mean ratio (+/- S.E.M.) between the fractional synthesis rates of muscle collagen and total protein was 0.99 +/- 0.10, where the total protein values were based on specific radioactivities of the homogenate free proline pools. 4. Types I, III and V collagen were solubilized by pepsin and isolated by fractional precipitation with NaCl. The fractional synthesis rates of types I and III collagens were very similar. Type V collagen samples had higher specific radioactivities than the other collagens, but this was not necessarily indicative of a higher rate of synthesis because of uncertainty about the cellular origin of this collagen and, hence, the specific radioactivity of its precursor proline pool.
D000818:Animals; D003094:Collagen / Q000096:biosynthesis*; D006909:Hydroxyproline / Q000378:metabolism; D007700:Kinetics; D009124:Muscle Proteins / Q000096:biosynthesis*; D009132:Muscles / Q000378:metabolism*; D010434:Pepsin A; D011347:Procollagen / Q000096:biosynthesis; D011392:Proline / Q000378:metabolism; D011817:Rabbits
D009124:Muscle Proteins; D011347:Procollagen; D003094:Collagen; D011392:Proline; D010434:Pepsin A; D006909:Hydroxyproline